|
|
| Line 1: |
Line 1: |
| [[Image:1g7e.gif|left|200px]] | | {{Seed}} |
| | [[Image:1g7e.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1g7e| PDB=1g7e | SCENE= }} | | {{STRUCTURE_1g7e| PDB=1g7e | SCENE= }} |
|
| |
|
| '''NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN'''
| | ===NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11435111}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11435111 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_11435111}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 1G7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7E OCA]. | | 1G7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7E OCA]. |
|
| |
|
| ==Reference== | | ==Reference== |
| Line 30: |
Line 34: |
| [[Category: Alfa-beta structure]] | | [[Category: Alfa-beta structure]] |
| [[Category: Thioredoxin fold]] | | [[Category: Thioredoxin fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:13:57 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:49:27 2008'' |
